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对由驱动蛋白运动结构域装饰的微管和薄片的极性进行重新检查。

Re-examination of the polarity of microtubules and sheets decorated with kinesin motor domain.

作者信息

Hirose K, Fan J, Amos L A

机构信息

MRC Laboratory of Molecular Biology, Cambridge, England.

出版信息

J Mol Biol. 1995 Aug 18;251(3):329-33. doi: 10.1006/jmbi.1995.0437.

Abstract

Electron microscope images of microtubules and tubulin sheets decorated with kinesin head domains have shown the main mass of the kinesin head domain to be superimposed on one subunit of each tubulin dimer. We have polymerized brain tubulin extensions on to the ends of flagellar axonemes under varied conditions, in order to check the polarity of the tubulin-kinesin head complex. Since the polarity of axonemes incubated with normal brain tubulin may be ambiguous, we also tried 50% N-ethylmaleimide-treated tubulin which specifically blocks minus ends. Our conclusion, which conflicts with recently published results, is that the main mass of the kinesin head is associated with the tubulin subunit closer to the plus end of a microtubule.

摘要

用驱动蛋白头部结构域修饰的微管和微管蛋白片层的电子显微镜图像显示,驱动蛋白头部结构域的主要部分叠加在每个微管蛋白二聚体的一个亚基上。我们在不同条件下将脑微管蛋白延伸段聚合到鞭毛轴丝的末端,以检查微管蛋白 - 驱动蛋白头部复合物的极性。由于用正常脑微管蛋白孵育的轴丝的极性可能不明确,我们还尝试了用50% N - 乙基马来酰亚胺处理的微管蛋白,它特异性地阻断负端。我们的结论与最近发表的结果相矛盾,即驱动蛋白头部的主要部分与更靠近微管正端的微管蛋白亚基相关联。

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